Biology:Death receptor 5

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Short description: Protein found in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Death receptor 5 (DR5), also known as TRAIL receptor 2 (TRAILR2) and tumor necrosis factor receptor superfamily member 10B (TNFRSF10B), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis.

Function

The protein encoded by this gene is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces apoptosis signal. Mice have a homologous gene, tnfrsf10b, that has been essential in the elucidation of the function of this gene in humans. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein.[1]

Interactions

DR5 has been shown to interact with:

Cancer therapy

Monoclonal antibodies targeting DR5 have been developed and are currently under clinical trials for patients suffer from a variety of cancer types, see Tigatuzumab (CS-1008).

Luminescent iridium complex-peptide hybrids, serving as TRAIL mimics, have been designed, which target the death receptors DR4 and DR5 on cancer cells and induce their apoptosis.[8]

See also

References

  1. "Entrez Gene: TNFRSF10B tumor necrosis factor receptor superfamily, member 10b". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8795. 
  2. 2.0 2.1 2.2 "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. Mar 2005. doi:10.1074/jbc.M411781200. PMID 15659383. 
  3. 3.0 3.1 "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL". J. Biol. Chem. 272 (41): 25417–20. Oct 1997. doi:10.1074/jbc.272.41.25417. PMID 9325248. 
  4. "Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway". Immunity 7 (6): 821–30. Dec 1997. doi:10.1016/s1074-7613(00)80400-8. PMID 9430227. 
  5. "Studies on the interaction between TWEAK and the death receptor WSL-1/TRAMP (DR3)". FEBS Lett. 485 (2–3): 135–41. Nov 2000. doi:10.1016/s0014-5793(00)02219-5. PMID 11094155. 
  6. "TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL". EMBO J. 16 (17): 5386–97. Sep 1997. doi:10.1093/emboj/16.17.5386. PMID 9311998. 
  7. "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5". Mol. Cell 4 (4): 563–71. Oct 1999. doi:10.1016/S1097-2765(00)80207-5. PMID 10549288. 
  8. "Design and synthesis of a luminescent iridium complex-peptide hybrid (IPH) that detects cancer cells and induces their apoptosis". Bioorganic & Medicinal Chemistry 26 (17): 4804–4816. September 2018. doi:10.1016/j.bmc.2018.08.016. PMID 30177492. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.